4.1.1.18	?	? * 80000, SDS-PAGE, under native conditions aggregation of up to 10 subunits	37283	
4.1.1.18	?	x * 24000, recombinant His-tagged enzyme, SDS-PAGE	749226	
4.1.1.18	?	x * 54800, recombinant His6-tagged enzyme, SDS-PAGE	748513	
4.1.1.18	?	x * 80000, equilibrium ultracentrifugation in 6 M guanidine-HCl, SDS-PAGE. Association of the dimeric form to the decamer is concomitant with the increase in ionic strength	-, 37289	
4.1.1.18	?	x * 80000, recombinant enzyme	-, 747594	
4.1.1.18	?	x * 80000, SDS-PAGE, high-speed sedimentation equilibrium in presence of 6 M guanidine HCl. Subunits associate or dissociate reversibly as a function of pH and ionic strength. The native decameric form is formed by the cyclic association of five dimers. Its overall appearance is that of two stacked pentameric rings. Higher aggregates result from the linear stacking of decamers to form rodlike particles of indefinite length	-, 37293	
4.1.1.18	?	x * 85000, SDS-PAGE	-, 727766	
4.1.1.18	decamer	-	748418	
4.1.1.18	decamer	10 * 80000, SDS-PAGE	37299	
4.1.1.18	decamer	10 * 81000, recombinant His-tagged wild-type and mutant T88S, SDS-PAGE	747396